Structure of PDB 2c6q Chain C

Receptor sequence

>2c6qC (length=328) Species: 9606 (Homo sapiens)

SLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTV
GTFEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSS
DFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGN
VVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADA
AHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIER
DGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDI
LGGIRSTCTYVGAAKLKELSRRTTFIRV

3D structure

• PDB: 2c6q Cofactor Mobility Determines Reaction Outcome in the Impdh and Gmpr (Beta-Alpha)(8) Barrel Enzymes.
• Chain: C
• Resolution: 1.7 Å

Enzymatic activity

• Enzyme Commision number: 1.7.1.7: GMP reductase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	IMP	C	M55 G183 S184 C186 D219 G220 G242 G243 G268 M269 S270 E289	M47 G175 S176 C178 D211 G212 G234 G235 G260 M261 S262 E281
BS02	NDP	C	T105 D129 V130 A131 I180 G181 T188 M269 S270 Y285 R286	T97 D121 V122 A123 I172 G173 T180 M261 S262 Y277 R278
BS03	NDP	C	K25 S26 R27 T317	K17 S18 R19 T309

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0003920 GMP reductase activity
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006144 purine nucleobase metabolic process
• GO:0006163 purine nucleotide metabolic process
• GO:0009117 nucleotide metabolic process
• GO:0046037 GMP metabolic process

Cellular Component

• GO:0005829 cytosol
• GO:1902560 GMP reductase complex

External links

• PDB: RCSB:2c6q, PDBe:2c6q, PDBj:2c6q
• PDBsum: 2c6q
• PubMed: 22037469
• UniProt: Q9P2T1|GMPR2_HUMAN GMP reductase 2 (Gene Name=GMPR2)